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Production of Minichaperone (sht GroEL191-345) and Its Function in the Refolding of Recombinant Human Interferon Gamma

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The recombinant minichaperone sht GroEL191-345 was cultivated in a 3.7 L stirred bioreactor with the high yield of 216.2 mg / L broth. In the refolding of recombinant human interferon gamma (rhuIFN-γ) inclusion bodies, more than 2-3 fold enhancement in protein mass recovery and total activity were observed in the presence of free or immobilized minichaperone to the refolding buffer.

Keywords: cultivation; minichaperone; purification; recombinant human interferon gamma; refolding; sht groel191-345

Document Type: Review Article


Affiliations: Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027 P. R. China.

Publication date: 2005-01-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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